Evidence map›Paper›PMID 27255832›Full record

ArticleScientific reports2016

Pro-apoptotic Bax molecules densely populate the edges of membrane pores.

Tomomi Kuwana, Norman H Olson, William B Kiosses, Bjoern Peters, Donald D Newmeyer

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Mechanism of membrane perforation in rotavirus cell entry.bioRxiv : the preprint server for biology · 2026
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  2. Review
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  6. Article
  7. Article
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  15. LncRNA HULC mediates radioresistance via autophagy in prostate cancer cells.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2018
    Article
  16. Review
  17. Article
  18. Pore formation by dimeric Bak and Bax: an unusual pore?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  19. Apoptotic foci at mitochondria: in and around Bax pores.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Tomomi KuwanaLa Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.
Norman H OlsonUniversity of California San Diego Cryo-EM Core Facility, La Jolla, CA 92037, USA.
William B KiossesLa Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.
Bjoern PetersLa Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.
Donald D NewmeyerLa Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.

Funding

Molecular mechanism of BCL2-dependent apoptosisR01CA179087 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HANEIN, DORIT, MARASSI, FRANCESCA M · 2014 to 2018
$3.6M
Mitochrondrial Regulation of ApoptosisR01GM086389 · NIGMS · UNIVERSITY OF IOWA · PI KUWANA, TOMOMI · 2009 to 2013
$1.6M
NCI NIH HHS R01 CA179087NIGMS NIH HHS R01 GM086389
6 · The paper itself

Abstract

How the pro-apoptotic Bax protein permeabilizes the mitochondrial outer membrane is not fully understood. Previously, using cryo-electron microscopy (cryo-EM), we showed that activated Bax forms large, growing pores. Whether formed in liposomes or in mitochondrial outer membranes, Bax-induced pores exhibit the same morphology, with negative curvature flanking the edges and with no visible protein structure protruding from the membranes. Here we used cryo-EM to show that gold-labeled Bax molecules, after activation by Bid, became localized strictly at pore edges. This argues that Bax acts at short range to deform the membrane. Also, Bax molecules populated the walls of both small and large pores at the same density, implying that Bax is continuously recruited to the pores as they widen. Moreover, because all Bax molecules became oligomerized after membrane insertion, we infer that Bax oligomers are present at pore edges. We suggest that oligomerization may promote pore enlargement.

Indexed as

PermeabilityApoptosis Regulatory Proteinsbcl-2-Associated X ProteinCryoelectron MicroscopyMitochondrial MembranesApoptosis Regulatory Proteinsbcl-2-Associated X Protein

Identifiers

PMID27255832
PMCPMC4891688

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.